Secretory expression in Bacillus subtilis, purification and characterization of a persistent protein-degrading enzyme from Nocardiopsis sp. TOA-1

Aoto Takano; Mamiko Yano; Tomoka Nakamura; Kazufumi Takano; Shun-Ichi Tanaka

doi:10.1093/bbb/zbae191

Secretory expression in Bacillus subtilis, purification and characterization of a persistent protein-degrading enzyme from Nocardiopsis sp. TOA-1

Biosci Biotechnol Biochem. 2024 Dec 10:zbae191. doi: 10.1093/bbb/zbae191. Online ahead of print.

Authors

Aoto Takano¹, Mamiko Yano¹, Tomoka Nakamura², Kazufumi Takano¹, Shun-Ichi Tanaka^{1

3}

Affiliations

¹ Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, 1-5 Shimogamohangi-cho, Sakyo-ku, Kyoto, Japan.
² Department of Biomolecular Chemistry, Kyoto Prefectural University, 1-5 Shimogamohangi-cho, Sakyo-ku, Kyoto, Japan.
³ Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, Japan.

PMID: 39658370
DOI: 10.1093/bbb/zbae191

Abstract

Keratinase from Nocardiopsis sp. TOA-1 (NAPase) holds significant potential for industrial and medical applications. Here, we developed a heterologous secretory expression system for NAPase in Bacillus subtilis. The recombinant enzyme exhibited catalytic properties comparable to the native enzyme, demonstrating its suitability for further protein engineering. This work provides a foundation for enhancing NAPase activity and stability, expediting its biotechnological applications.

Keywords: Bacillus subtilis; Nocardiopsis sp; Alkaline protease; Keratinase; protein engineering.